ID PKN2_CLOAB Reviewed; 657 AA. AC Q97IC2; DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 02-SEP-2026, entry version 131. DE RecName: Full=Probable serine/threonine-protein kinase CA_C1728; DE EC=2.7.11.1; GN OrderedLocusNames=CA_C1728; OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM OS 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W). OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=272562; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC RC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W; RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001; RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., RA Smith D.R.; RT "Genome sequence and comparative analysis of the solvent-producing RT bacterium Clostridium acetobutylicum."; RL J. Bacteriol. 183:4823-4838(2001). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE001437; AAK79694.1; -; Genomic_DNA. DR PIR; C97113; C97113. DR RefSeq; WP_010965035.1; NC_003030.1. DR AlphaFoldDB; Q97IC2; -. DR SMR; Q97IC2; -. DR STRING; 272562.CA_C1728; -. DR GeneID; 44998223; -. DR KEGG; cac:CA_C1728; -. DR PATRIC; fig|272562.8.peg.1930; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2815; Bacteria. DR HOGENOM; CLU_000288_135_2_9; -. DR OrthoDB; 9788659at2; -. DR Proteomes; UP000000814; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR CDD; cd06577; PASTA_pknB; 3. DR CDD; cd14014; STKc_PknB_like; 1. DR FunFam; 1.10.510.10:FF:000021; Serine/threonine protein kinase; 1. DR FunFam; 3.30.200.20:FF:000035; Serine/threonine protein kinase Stk1; 1. DR Gene3D; 3.30.10.20; -; 3. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR005543; PASTA_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR NCBIfam; NF033483; PknB_PASTA_kin; 1. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF34; SERINE_THREONINE-PROTEIN KINASE YBDM-RELATED; 1. DR Pfam; PF03793; PASTA; 3. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00740; PASTA; 3. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51178; PASTA; 3. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..657 FT /note="Probable serine/threonine-protein kinase CA_C1728" FT /id="PRO_0000171194" FT DOMAIN 10..274 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 375..441 FT /note="PASTA 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528" FT DOMAIN 443..509 FT /note="PASTA 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528" FT DOMAIN 512..577 FT /note="PASTA 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528" FT REGION 286..334 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 581..657 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 288..298 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 584..600 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 613..637 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 645..657 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 143 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 16..24 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 657 AA; 71115 MW; 0901452EF42E2CA6 CRC64; MIGTVLSNRY KIEEEIGVGG TAVVYKAMDT LLNRHVAVKV LKHEFTEDEE FVFKFKREAS AAARIANANI VNIYDVGADG NVNYIVMEYV AGKTLKKLIK ENGKIEFNKI IDYATQIAKA LNFAHKNGIV HRDIKPHNIM VTDDDIIKVT DFGIAKASNE STITTTNKVV GSAHYLSPEQ AQGIPVDCRT DIYSFGIVLY EMATGKVPYD ADTPVSIALK HIQDAAVPPN ELNKDIPIAL NKMILRCIEK KPENRYQNAN EILDELSNVK NNYVNDDEEF TRVMDPAQIQ NESNPNNKLD NDDTYYNGEP YNKEQPQEEP QEENEEPKNK IKGNNMLSGK AKKALVASII VVLILAGSAL AFSMGSGIFK PNSNSVSKVK VPKIIGLSES DAKGKVEDAK LKFQVVDRVK SSKPKGTVVT CYPNEDTEVD SGTVVRVDIS SGDTDQTLPS LVGLPESAAR AQIKQYGCNV GSVTQEYSDD VAQGNVISQS PSEGSQIKKG MTIDLVISRG PEVKKATVPS VYGKTSDSAS SILQNAGFGV NVQNKDVTNA DQNGIVIEEY PNGYVNKGTT VTIVIGRFNS TAVQPPNNNN GNGNQNQNQN KTPDTNHDDS KAPTGGNNDN QNQNNTTNPN GTQPAGGNVT GTGNGNVTNT PNGTGQK //